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Prepublished online as a Blood First Edition Paper on February 6, 2003; DOI 10.1182/blood-2002-10-3076. This Article Full Text (PDF) All Versions of this Article: 2002-10-3076v1 101/11/4628    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Lobo, C. A Articles by Lustigman, S. Search for Related Content PubMed PubMed Citation Articles by Lobo, C. A Articles by Lustigman, S. Social Bookmarking                   What's this? Submitted October 9, 2002 Accepted January 28, 2003 Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl) Cheryl A Lobo*, Marilis Rodriguez, Marion Reid, and Sara Lustigman Molecular Parasitology, The Lindsley Kimball Research Institute, New York, NY, USA Immunohematology, Lindsley Kimball Research Institute, New York, NY, USA * Corresponding author; email: cheryl_lobo{at}nybc.org. We report in this paper that Glycophorin C (GPC) is the receptor for PfEBP-2 (baebl, EBA-140), the newly identified erythrocyte binding ligand of Plasmodium falciparum. PfEBP-2 is a member of the Duffy binding like-erythrocyte binding protein (DBL-EBP) family. Although several reports have been published characterizing PfEBP-2, the identity of its erythrocytic receptor was still unknown. Using a combination of enzymatically treated red blood cells and rare, variant red blood cells lacking different surface proteins we have shown that PfEBP-2 does not bind to cells lacking GPC. Additionally, we found that PfEBP-2 binds differentially to variants of GPC, lacking exon 2 or exon 3, and determined that the binding domain on GPC is potentially restricted to amino acid residues 14-22 within exon 2. Thus PfEBP-2 is involved in a sialic acid-dependent pathway of invasion, which does not involve GPA or GPB and represents a novel route of entry into the RBC. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: L. Ford, C. A. Lobo, M. Rodriguez, M. G. Zalis, R. L. D. Machado, A. R. B. Rossit, C. E. Cavasini, A. A. R. Couto, P. A. Enyong, and S. 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